SPL_BACSU
ID SPL_BACSU Reviewed; 342 AA.
AC P37956;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Spore photoproduct lyase;
DE EC=4.1.99.14;
GN Name=splB; Synonyms=spl; OrderedLocusNames=BSU13930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8449881; DOI=10.1128/jb.175.6.1735-1744.1993;
RA Fajardo-Cavazos P., Salazar C., Nicholson W.L.;
RT "Molecular cloning and characterization of the Bacillus subtilis spore
RT photoproduct lyase (spl) gene, which is involved in repair of UV radiation-
RT induced DNA damage during spore germination.";
RL J. Bacteriol. 175:1735-1744(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-342.
RC STRAIN=168;
RX PubMed=9353924; DOI=10.1099/00221287-143-10-3231;
RA Mueller J., Schiel S., Ordal G.W., Saxild H.H.;
RT "Functional and genetic characterization of mcpC, which encodes a third
RT methyl-accepting chemotaxis protein in Bacillus subtilis.";
RL Microbiology 143:3231-3240(1997).
RN [4]
RP DEVELOPMENTAL STAGE.
RC STRAIN=168;
RX PubMed=8021181; DOI=10.1128/jb.176.13.3983-3991.1994;
RA Pedraza-Reyes M., Gutierrez-Corona F., Nicholson W.L.;
RT "Temporal regulation and forespore-specific expression of the spore
RT photoproduct lyase gene by sigma-G RNA polymerase during Bacillus subtilis
RT sporulation.";
RL J. Bacteriol. 176:3983-3991(1994).
RN [5]
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=11470912; DOI=10.1073/pnas.161278998;
RA Rebeil R., Nicholson W.L.;
RT "The subunit structure and catalytic mechanism of the Bacillus subtilis DNA
RT repair enzyme spore photoproduct lyase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9038-9043(2001).
RN [6]
RP REACTION MECHANISM.
RX PubMed=11902862; DOI=10.1021/ja017784g;
RA Cheek J., Broderick J.B.;
RT "Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair
RT in the reaction catalyzed by spore photoproduct lyase: evidence for a
RT reversibly generated adenosyl radical intermediate.";
RL J. Am. Chem. Soc. 124:2860-2861(2002).
RN [7]
RP MUTAGENESIS OF CYS-91; CYS-95; CYS-98 AND CYS-141.
RX PubMed=16163454; DOI=10.1007/s00284-005-0052-8;
RA Fajardo-Cavazos P., Rebeil R., Nicholson W.L.;
RT "Essential cysteine residues in Bacillus subtilis spore photoproduct lyase
RT identified by alanine scanning mutagenesis.";
RL Curr. Microbiol. 51:331-335(2005).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=16493831; DOI=10.1039/b514103f;
RA Friedel M.G., Berteau O., Pieck J.C., Atta M., Ollagnier-de-Choudens S.,
RA Fontecave M., Carell T.;
RT "The spore photoproduct lyase repairs the 5S- and not the 5R-configured
RT spore photoproduct DNA lesion.";
RL Chem. Commun. (Camb.) 4:445-447(2006).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=168 / JH624 / KI1152;
RX PubMed=16829680; DOI=10.1074/jbc.m603931200;
RA Buis J.M., Cheek J., Kalliri E., Broderick J.B.;
RT "Characterization of an active spore photoproduct lyase, a DNA repair
RT enzyme in the radical S-adenosylmethionine superfamily.";
RL J. Biol. Chem. 281:25994-26003(2006).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16829676; DOI=10.1074/jbc.m602297200;
RA Chandor A., Berteau O., Douki T., Gasparutto D., Sanakis Y.,
RA Ollagnier-de-Choudens S., Atta M., Fontecave M.;
RT "Dinucleotide spore photoproduct, a minimal substrate of the DNA repair
RT spore photoproduct lyase enzyme from Bacillus subtilis.";
RL J. Biol. Chem. 281:26922-26931(2006).
RN [11]
RP MUTAGENESIS OF CYS-141, AND REACTION MECHANISM.
RX PubMed=18957420; DOI=10.1074/jbc.m806503200;
RA Chandor-Proust A., Berteau O., Douki T., Gasparutto D.,
RA Ollagnier-de-Choudens S., Fontecave M., Atta M.;
RT "DNA repair and free radicals, new insights into the mechanism of spore
RT photoproduct lyase revealed by single amino acid substitution.";
RL J. Biol. Chem. 283:36361-36368(2008).
CC -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage during
CC spore germination. Can repair thymine dimer 5-thyminyl-5,6-
CC dihydrothymine (known as spore photoproduct (SP)) by in situ
CC monomerization of SP to two thymines. {ECO:0000269|PubMed:16829676,
CC ECO:0000269|PubMed:16829680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine in DNA = a
CC thymidine dimer in DNA; Xref=Rhea:RHEA:56132, Rhea:RHEA-COMP:14387,
CC Rhea:RHEA-COMP:14449, ChEBI:CHEBI:139518, ChEBI:CHEBI:139519;
CC EC=4.1.99.14; Evidence={ECO:0000269|PubMed:11470912,
CC ECO:0000269|PubMed:16493831, ECO:0000269|PubMed:16829676,
CC ECO:0000269|PubMed:16829680};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.;
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Note=Binds 1 S-adenosyl-L-methionine per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for SPTpT {ECO:0000269|PubMed:16829676};
CC Note=SPTpT is the spore photoproduct of the TpT dinucleoside.;
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:11470912,
CC ECO:0000269|PubMed:16829676, ECO:0000269|PubMed:16829680}.
CC -!- DEVELOPMENTAL STAGE: Expressed at stage III of sporulation in the
CC forespore compartment of the developing sporangium.
CC {ECO:0000269|PubMed:8021181}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. SPL family.
CC {ECO:0000305}.
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DR EMBL; L08809; AAA22416.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13266.1; -; Genomic_DNA.
DR EMBL; X97385; CAA66050.1; -; Genomic_DNA.
DR PIR; C47084; C47084.
DR RefSeq; NP_389276.1; NC_000964.3.
DR RefSeq; WP_003245173.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P37956; -.
DR SMR; P37956; -.
DR STRING; 224308.BSU13930; -.
DR PaxDb; P37956; -.
DR PRIDE; P37956; -.
DR DNASU; 939248; -.
DR EnsemblBacteria; CAB13266; CAB13266; BSU_13930.
DR GeneID; 939248; -.
DR KEGG; bsu:BSU13930; -.
DR PATRIC; fig|224308.179.peg.1519; -.
DR eggNOG; COG1533; Bacteria.
DR InParanoid; P37956; -.
DR OMA; HCQYCYL; -.
DR PhylomeDB; P37956; -.
DR BioCyc; BSUB:BSU13930-MON; -.
DR BioCyc; MetaCyc:MON-15020; -.
DR BRENDA; 4.1.99.14; 658.
DR SABIO-RK; P37956; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042601; C:endospore-forming forespore; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003913; F:DNA photolyase activity; IDA:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023897; Spore_PP_lysase.
DR InterPro; IPR034560; Spore_PP_lysase_Bacilli.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDF00292; spore_photoproduct_lyase_1; 1.
DR TIGRFAMs; TIGR04070; photo_TT_lyase; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA damage; DNA repair; DNA-binding; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; Sporulation.
FT CHAIN 1..342
FT /note="Spore photoproduct lyase"
FT /id="PRO_0000085124"
FT DOMAIN 77..305
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DNA_BIND 218..235
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT MUTAGEN 91
FT /note="C->A: No activity. No iron-sulfur cluster formed."
FT /evidence="ECO:0000269|PubMed:16163454"
FT MUTAGEN 95
FT /note="C->A: No activity. No iron-sulfur cluster formed."
FT /evidence="ECO:0000269|PubMed:16163454"
FT MUTAGEN 98
FT /note="C->A: No activity. No iron-sulfur cluster formed."
FT /evidence="ECO:0000269|PubMed:16163454"
FT MUTAGEN 141
FT /note="C->A: Performs first half of the reaction. No effect
FT on iron-sulfur cluster formation."
FT /evidence="ECO:0000269|PubMed:16163454,
FT ECO:0000269|PubMed:18957420"
SQ SEQUENCE 342 AA; 39943 MW; 9AF96E7C7C52FEBF CRC64;
MQNPFVPQLV YIEPRALEYP LGQELQDKFE NMGIEIRETT SHNQVRNIPG KNHLQQYRNA
KSTLVIGVRK TLKFDSSKPS AEYAIPFATG CMGHCHYCYL QTTMGSKPYI RTYVNVEEIL
DQADKYMKER APEFTRFEAS CTSDIVGIDH LTHTLKRAIE HFGQSDLGKL RFVTKFHHVD
HLLDAKHNGK TRFRFSINAD YVIKNFEPGT SPLDKRIEAA VKVAKAGYPL GFIVAPIYIH
EGWEEGYRHL FEKLDAALPQ DVRHDITFEL IQHRFTKPAK RVIEKNYPKT KLELDEEKRR
YKWGRYGIGK YIYQKDEEHA LREALESYID TFFPNAKIEY FT
